Comparison of the interfacial properties of native and refolded myofibrillar proteins subjected to pH-shifting.

The emulsion abilities of pale, soft, exudative (PSE)-like chicken breast protein are unsatisfied, which are urgently needed to be ameliorated. This study evaluated the improvement of pH-shifting (11.0-, 11.5- and 12.0-7.0) on emulsion properties of the PSE-like chicken breast myofibrillar proteins (MPs) and the underlined structure-driven interfacial mechanism. It was found pH-shifting promoted the exposure of buried hydrophobic groups and free sulfhydryl groups, and changed secondary structures. Emulsions stabilized by refolded MPs exhibited more uniform and dispersed distributions with more adsorbed proteins at the interface. Electrophorogram showed both disulfide and non-disulfide covalent bonds were involved during interfacial protein-protein interaction. The results from circular dichroism and front-surface fluorescence spectroscopy revealed interfacial MPs were exposed to a more hydrophobic environment and increased β-sheets enhanced their molecular interactions. In addition, interfacial proteins after pH-shifting was less likely to be replaced by Tween 20.